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Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli

U Hermanns1, P Sebbel, V Eggli

  • 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, CH-8093 Zürich, Switzerland.

Biochemistry
|September 20, 2000
PubMed

Insights

This study characterizes FimC, a crucial chaperone for assembling Escherichia coli type 1 pili. It reveals strong interdomain interactions within FimC and specific binding to folded pilus subunits, not just C-terminal segments.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Type 1 pili assembly in Escherichia coli relies on the periplasmic chaperone FimC.
  • FimC is believed to interact with pilus subunits via their C-terminal regions for delivery to the outer membrane assembly platform.

Purpose of the Study:

  • To biochemically characterize the periplasmic pilus chaperone FimC.
  • To investigate the role of FimC's two immunoglobulin-like domains in stability and function.

Main Methods:

  • Biochemical characterization of wild-type FimC and its isolated C-terminal domain.
  • Thermodynamic stability analysis.
  • Binding affinity assays using peptides and intact pilus subunits.

Main Results:

  • Isolated C-terminal domain of FimC showed significantly reduced thermodynamic stability compared to the intact chaperone.
  • Strong interdomain interactions were inferred within the FimC structure.
  • FimC exhibited at least a 1000-fold lower binding affinity for a C-terminal peptide of FimH compared to intact FimH.

Conclusions:

  • Bacterial pilus chaperones, including FimC, demonstrate specific interactions with folded pilus subunits.
  • Interdomain interactions within FimC are critical for its stability and likely its function in pilus assembly.

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